Decreased intracellular proteolysis correlates with the maintenance of a specific isoenzyme of cytochrome P-450

Evans, Peter J. 1999. Decreased intracellular proteolysis correlates with the maintenance of a specific isoenzyme of cytochrome P-450. Cell Biology International 23 (2) , pp. 117-124. 10.1006/cbir.1998.0333

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Abstract

The rates of intracellular protein degradation, of identically labelled populations of proteins, were compared in hepatocytes cultured at 37° (on an adsorbed collagen layer) and in cells preserved on gelatin gels at 10°C. The half-lives of the long-lived proteins were 35.4±8.6h (N=4) and 692.9±216.9h (N=4) respectively. Proteolysis was substantially decreased at 10°C but the rate of decrease remained constant. Hepatocytes rapidly removed resorufin from the culture medium. The resorufin was not being conjugated or accumulated within the cells. Dicumarol, a potent inhibitor of quinone oxidoreductase, at high concentration (500μm) caused only a 72% decrease in the utilization of resorufin. The microsomal detoxifying enzyme, cytochrome P-450 1A1 remained at a constant level in the preserved hepatocyte monolayers. The results of this study strongly favour storing hepatocytes at 10°C rather than at 4° or 37°C.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Biosciences
Subjects:	Q Science > Q Science (General)
Uncontrolled Keywords:	Hepatocytes; preservation; intracellular protein degradation; cytochrome P-450 1A1.
Publisher:	Wiley
ISSN:	1065-6995
Last Modified:	28 Jun 2019 02:01
URI:	https://orca.cardiff.ac.uk/id/eprint/63351

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